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• W2169356930 endingPage "1807" @default.
• W2169356930 startingPage "1787" @default.
• W2169356930 abstract "Effective treatment of Alzheimer's disease (AD) remains a critical unmet need in medicine. The lack of useful treatment for AD led to an intense search for novel therapies based on the amyloid hypothesis, which states that amyloid β-42 (Aβ42) plays an early and crucial role in all cases of AD. β-Secretase (also known as BACE-1 β-site APP-cleaving enzyme, Asp-2 or memapsin-2) is an aspartyl protease representing the rate limiting step in the generation of Aβ peptide fragments, therefore it could represent an important target in the steady hunt for a disease-modifying treatment. Generally, β-secretase inhibitors are grouped into two families: peptidomimetic and nonpeptidomimetic inhibitors. However, irrespective of the class, serious challenges with respect to blood-brain barrier (BBB) penetration and selectivity still remain. Discovering a small molecule inhibitor of β-secretase represents an unnerving challenge but, due to its significant potential as a therapeutic target, growing efforts in this task are evident from both academic and industrial laboratories. In this frame, the rising availability of crystal structures of β-secretase-inhibitor complexes represents an invaluable opportunity for optimization. Nevertheless, beyond the inhibitory activity, the major issue of the current research approaches is about problems associated with BBB penetration and pharmacokinetic properties. This review follows the structural evolution of the early β-secretase inhibitors and gives a snap-shot of the hottest chemical templates in the literature of the last five years, showing research progress in this field." @default.
• W2169356930 created "2016-06-24" @default.
• W2169356930 creator A5004950855 @default.
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• W2169356930 creator A5060371306 @default.
• W2169356930 creator A5079124576 @default.
• W2169356930 creator A5084867757 @default.
• W2169356930 date "2013-07-31" @default.
• W2169356930 modified "2023-09-27" @default.
• W2169356930 title "The Structural Evolution of &#946;-Secretase Inhibitors: A Focus on the Development of Small-Molecule Inhibitors" @default.
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